| Activity |
|---|
| Catalytic type | Aspartic |
| Peplist | Included in the Peplist with identifier PL00005 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.15
|
| Enzymology | BRENDA database |
| Activity | Cleaves near the N-terminus of the protein angiotensinogen to release angiotensin I. |
| Proteolytic events | CutDB database (2 cleavages) |
| Activity status | human: active (Suzuki et al., 2004)
mouse: active (Hansen et al., 2004)
|
| Inhibitors | Not trapped by alpha-2-macroglobulin (Barrett 1981). |
| Physiology | Liberated from kidney into the plasma, renin plays a central role in controlling blood pressure as it catalyzes the first step in the production of angiotensin II, release of angiotensin I from angiotensinogen (Fuchs et al., 2002). Angiotensin I is subsequently converted to the hypertensive peptide angiotensin II by the action of angiotensin-converting enzyme (XM02-001). |
| Knockout | A variety of transgenic models have been used in the investigation of the functions of renin (Lavoie & Sigmund, 2003). |
| Pharmaceutical relevance | Inhibitors of renin lower blood pressure in some forms of hypertension, and are being studied for their potential as drugs in the management of high blood pressure (Leckie, 2005). A drug in a late stage of development is aliskiren. |
| Pathways |
KEGG | Renin-angiotensin system |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Renin |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | P/F/H/L Lvk/viy/Yhg/Sn (based on 10 cleavages) |
